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Database: UniProt
Entry: A0A091Q8B7_LEPDC
LinkDB: A0A091Q8B7_LEPDC
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ID   A0A091Q8B7_LEPDC        Unreviewed;       392 AA.
AC   A0A091Q8B7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 20.
DE   RecName: Full=alpha-L-fucosidase {ECO:0000256|ARBA:ARBA00012662};
DE            EC=3.2.1.51 {ECO:0000256|ARBA:ARBA00012662};
DE   Flags: Fragment;
GN   ORFNames=N330_14556 {ECO:0000313|EMBL:KFQ15806.1};
OS   Leptosomus discolor (Madagascar cuckoo roller) (Cuculus discolor).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Coraciiformes; Leptosomidae; Leptosomus.
OX   NCBI_TaxID=188344 {ECO:0000313|EMBL:KFQ15806.1, ECO:0000313|Proteomes:UP000053001};
RN   [1] {ECO:0000313|EMBL:KFQ15806.1, ECO:0000313|Proteomes:UP000053001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N330 {ECO:0000313|EMBL:KFQ15806.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-
CC       1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the
CC       carbohydrate moieties of glycoproteins.
CC       {ECO:0000256|ARBA:ARBA00004071}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a neolactoside IV(2)-alpha-Fuc-nLc4Cer(d18:0) + H2O = a
CC         neolactoside nLc4Cer(d18:0) + L-fucose; Xref=Rhea:RHEA:49308,
CC         ChEBI:CHEBI:2181, ChEBI:CHEBI:15377, ChEBI:CHEBI:91119,
CC         ChEBI:CHEBI:91121; Evidence={ECO:0000256|ARBA:ARBA00000419};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49309;
CC         Evidence={ECO:0000256|ARBA:ARBA00000419};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a neolactoside IV(2)-alpha-Fuc-nLc4Cer(d18:1(4E)) + H2O = a
CC         neolactoside nLc4Cer(d18:1(4E)) + L-fucose; Xref=Rhea:RHEA:48224,
CC         ChEBI:CHEBI:2181, ChEBI:CHEBI:15377, ChEBI:CHEBI:17006,
CC         ChEBI:CHEBI:28691; Evidence={ECO:0000256|ARBA:ARBA00000321};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48225;
CC         Evidence={ECO:0000256|ARBA:ARBA00000321};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 29 family.
CC       {ECO:0000256|ARBA:ARBA00007951}.
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DR   EMBL; KK688968; KFQ15806.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091Q8B7; -.
DR   PhylomeDB; A0A091Q8B7; -.
DR   Proteomes; UP000053001; Unassembled WGS sequence.
DR   GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006004; P:fucose metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR016286; FUC_metazoa-typ.
DR   InterPro; IPR031919; Fucosidase_C.
DR   InterPro; IPR000933; Glyco_hydro_29.
DR   InterPro; IPR018526; Glyco_hydro_29_CS.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10030; ALPHA-L-FUCOSIDASE; 1.
DR   PANTHER; PTHR10030:SF45; PLASMA ALPHA-L-FUCOSIDASE; 1.
DR   Pfam; PF01120; Alpha_L_fucos; 1.
DR   Pfam; PF16757; Fucosidase_C; 1.
DR   PIRSF; PIRSF001092; Alpha-L-fucosidase; 1.
DR   PRINTS; PR00741; GLHYDRLASE29.
DR   SMART; SM00812; Alpha_L_fucos; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00385; ALPHA_L_FUCOSIDASE; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053001};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          301..389
FT                   /note="Alpha-L-fucosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16757"
FT   SITE            219
FT                   /note="May be important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001092-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ15806.1"
FT   NON_TER         392
FT                   /evidence="ECO:0000313|EMBL:KFQ15806.1"
SQ   SEQUENCE   392 AA;  45030 MW;  7057CB7FB4EDAA24 CRC64;
     WYWQKEKRAP YVKFMEANYP PGFSYEDFGP LFTAEFFDPN QWADILKASG AKYVVLTSKH
     HEGFTLWGSK YSWNWNAVDV GPKRDLVAEL ATSVRNRTDL RFGLYHSLFE WFNPLFLEDA
     TNVFKTRKFP TSKSLPELYE IVTKYQPEII WSDGNGNAPD TYWNSTGFLA WLYNDSPVRD
     TVVTNDRWGV GSICTHGGFY TCSDRYNPGH LLPHKWENCM TIDKRSWGYR RNAQLDDYLT
     IEDLVKQLVE TVSCGGNLLM NIGPTHDGHI AVVFEERLRQ MGAWLKVNGD AIYGTKPWRA
     QNDTITPGVW YTFSPKEGKV NAIFLNWPVS GTLELGEPQA KLGETQVKLL GYKELLKWVA
     LGEKGIVIVL PQLTLKQLPC QWGWTLQLTD IN
//
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